Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CASEIN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 955 records · Page 53Linked to original sources
PubMed1976

Possible interaction of cyclic nucleotides with the prolactin stimulation of casein synthesis in mouse mammary gland explants.

During a 10-h incubation, cyclic nucleotide phosphodiesterase inhibitors, viz. theophylline and quinine, were found to reduce by 40-50% the rate of [3H] leucine incorporation into casein in mammary gland explants from midpregnant mice. Further, dibutyryl cyclic AMP as well as the phosphodiesterase inhibitors were found to abolish the prolactin stimulation of leucine incorporation into casein. Elevated levels of cyclic AMP therefore appear to impair the functionality of the mammary gland. Although cyclic GMP was previously shown to stimulate RNA synthesis in the mammary gland in a prolactin-like manner, it had no effect on the rate of casein synthesis in mammary gland explants. Preincubation of explants with cyclic GMP did, however, attenuate the time required for the commencement of the prolactin stimulation of the rate of leucine incorporation into casein. A physiological role of cyclic GMP for the regulation of the rate of casein synthesis is thus suggested.

Animals↗
PubMed1977

Purification and some physicochemical properties of bovine kappa-casein.

1. A description is given of the fractionation of kappa-casein on DEAE-cellulose using a pH gradient. With this method an improved separation of the kappa-casein components with a higher negative charge is obtained. 2. It is shown that at least one of the kappa-casein fractions has a second phosphate ester group. The heterogeneity of kappa-casein therefore is not exclusively caused by a varying N-acetylneuraminic acid content. 3. Ultracentrifuge experiments and exclusion gel chromatography show that the purified kappa-casein fraction having the lowest electrophoretic mobility exhibits a monomer-polymer association equilibrium. The free energy of association per mol monomer in 0.2 M NaCl is approximately --36 kJ-mol-1.

Animals↗
PubMed1990

Phosphorylation of src-phosphopeptides by casein kinases-1 and -2: favourable effect of phosphotyrosine.

The synthetic phosphotyrosyl tridecapeptide H-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg-Gln-Gly-OH, reproducing a major phosphoacceptor site of protein tyrosine kinases of the src-family, can be phosphorylated at Thr-9 by both casein kinases -1 and -2. Its shorter derivative H-Asn-Glu-Tyr(P)-Thr-Ala-OH is not affected by casein kinase-1 while representing a substrate as good as the tridecapeptide for casein kinase-2. The unphosphorylated analogue H-Asn-Glu-Tyr-Thr-Ala-OH, however, is a much poorer substrate, and no significant phosphorylation could be observed of its O-methyl ether derivative H-Asn-Glu-Tyr(Me)-Thr-Ala-OMe. These data on one side corroborate the concept that casein kinase-1 recognizes residues located on the C-terminal edge of acidic stretches, providing, on the other, the evidence that phosphotyrosyl side chains can act as specificity determinants for casein kinase-2.

Amino Acid Sequence↗
PubMed1985

Preparation and amino acid sequence of human kappa-casein.

Human kappa-casein was prepared from whole casein by successive hydroxyapatite and thiol-Sepharose chromatographies. The primary structure of its 99-residue N-terminal fragment has been determined by sequencing peptides obtained by tryptic and chymotryptic digestions of the whole protein. This fragment overlaps the known sequence of the 65-residue C-terminal fragment. The 158-residue sequence of human kappa-casein was compared to those of goat, ewe, cow and rat kappa-caseins. Only 22% of the residues are identical in homologous positions. The rate of divergence of the 93-residue N-terminal segment (para-kappa-casein) appears to be higher than that of the rest of the molecule.

Amino Acid Sequence↗
PubMed1990

Cloning and sequencing of a cDNA encoding human milk beta-casein.

A cDNA of 1065 bp encoding the human milk beta-casein was cloned and sequenced using a synthetic oligodeoxyribonucleotide probe and a human mammary gland library. The nucleotide (nt) sequence contained an open reading frame sufficient to encode the entire amino-acid (aa) sequence of a beta-casein precursor protein consisting of 210 aa and a signal peptide of 15 aa. The nt sequence shows 45-62% homology to those of bovine, ovine, rat, and mouse beta-caseins. The highly phosphorylated site, which is responsible for the calcium-binding capacity of beta-casein, the signal peptide, and a sequence encoding for an inhibitor to the angiotensin-converting enzyme seem highly conserved among the beta-caseins with known sequences.

Amino Acid Sequence↗
PubMed1992

Phosphorylation of the phosphatase modulator subunit (inhibitor-2) by casein kinase-1. Identification of the phosphorylation sites.

The isolated modulator subunit of the inactive protein phosphatase-1 is phosphorylated in vitro by casein kinase-1 at two different sites: Ser-86 and Ser-174. The Ser-86 site is a common target for casein kinase-1 and casein kinase-2, but is preferentially phosphorylated by the former enzyme. The Ser-174 site seems to be specific for casein kinase-1, and is phosphorylated at a slower rate. These results give a new insight into the in vitro phosphorylation pattern of the modulator subunit of the phosphatase and provides additional data on the specificity of casein kinase-1.

Amino Acid Sequence↗
PubMed1982

Comparison between the hypercholesterolaemia in rabbits induced by semipurified diets containing either cholesterol or casein.

Rabbits were fed a semipurified diet containing soy protein for 4 weeks and subsequently transferred to a semipurified diet containing soy protein plus cholesterol (2 g/kg), or a semipurified diet containing casein as protein source. One group of rabbits was fed the soy protein diet throughout the entire experimental period. Blood samples from the animals were taken after an overnight fast. The rabbits transferred to the soy plus cholesterol diet and to the casein diet showed a significant increase in serum cholesterol concentration after 1 and 3 days, respectively. The cholesterol and protein content of the LDL1 (1.019 less than p20 less than 1.040) fraction was markedly increased after 3 days on the casein and soy plus cholesterol diets. Thereafter the cholesterol, but not the protein concentration increased in the IDL1 (1.006 less than p20 less than 1.012) and VLDL (p20 less than 1.006) fractions, the effect being earlier and more pronounced in the soy plus cholesterol-fed animals. When compared to the soy-fed animals, the casein and soy plus cholesterol-fed animals showed a marked increase in the apoprotein E content of their VLDL and IDL fractions. It is concluded that cholesterol- and casein-induced hypercholesterolaemia in rabbits develop in a similar manner. In both hypercholesterolaemias the cholesterol concentration increases first in the LDL fraction and subsequently in the IDL and VLDL fractions.

Animals↗
PubMed1984

The effect of dietary casein and soy protein on cholesterol and very low density lipoprotein metabolism in the rat.

Rats fed a high-cholesterol semipurified diet containing casein developed higher levels of serum cholesterol than soy-fed animals. The hypercholesterolaemia of casein-fed rats was due to accumulation of very low density lipoproteins (VLDL), as measured by increased concentrations of serum VLDL cholesterol, protein and apoprotein B. High density lipoprotein (HDL) cholesterol was similar for the two dietary groups. Cholesterol absorption, as measured by the dual isotope ratio method and by direct measurement of cholesterol secretion into thoracic duct lymph, did not differ between the two groups. Cholesterol kinetics were derived from plasma cholesterol specific radioactivity curves and the casein-fed rats had a similar rate of plasma cholesterol production, but a significantly lower plasma cholesterol fractional catabolic rate (FCR) compared with the soy-fed rats. Kinetics of plasma VLDL apoprotein B, derived from analysis of reinjected 125I-labelled VLDL protein, also showed a lower fractional catabolic rate with casein feeding. This suggests that the accumulation of VLDL in the plasma of rats fed dietary casein is not due to excess VLDL production but to deficient VLDL removal. The hypercholesterolaemia appears to be a consequence of diminished VLDL catabolism.

Animals↗
PubMed1977

A sensitive radioimmunoassay for a component of mouse casein.

Mouse casein (m.w. 22,000 daltons) has been purified by employing Sephadex G-100 and DEAE-cellulose column chromatographies. A sensitive radioimmunoassay method has been developed by using [125I]-labelled casein and antiserum elicited in rabbits after injection of glutaraldehyde-treated casein. The assay method is capable of detecting as little as 0.1 ng of casein. The use of the present radioimmunoassay method in detecting casein production in cultured mouse mammary explants has also been demonstrated.

Animals↗
PubMed1987

Substitution of mixed amino acids resembling soy protein for mixed amino acids resembling casein in the diet reduces plasma cholesterol in slowly, but not rapidly fed nor fasted baboons.

Studies of cholesterol and triglyceride metabolism were conducted under steady-state conditions in conscious restrained female baboons to ascertain whether the cholesterol- and triglyceride-lowering effects of soy protein v casein in nonrodents can be explained by differences in amino acid composition between the two proteins and whether the lipid-lowering effects of soy protein are influenced by fasting or the rate of feeding, ie, the nutritional state. The metabolic changes underlying the changes in serum cholesterol and triglyceride concentration were also investigated. Isocaloric diets consisting of 45% mixed amino acids (soy or casein type), 50% glucose and 5% corn oil, including all nutritional requirements, were infused intraduodenally for five days. There were no differences in lipid levels between the soy and casein diets in fasting baboons (days 4 or 5) or when the daily diet (calculated to equal 24 hours of energy utilization) was given rapidly by constant intraduodenal infusion over seven hours (day 4). During rapid feeding there was, unexpectedly, no significant change in plasma cholesterol concentration, but the estimated rate of cholesterol oxidation to bile acids fell significantly by 38 +/- 6% (from 39 +/- 4 to 24 +/- 3 mg/d). Significant differences between the soy and casein diets were observed only in the fed state produced by the slow constant isocaloric intraduodenal infusions of the diets [5.8 mg mixed amino acids (soy or casein type) plus 7.2 mg glucose/min/kg body wt0.75] on day 5. These diets were calculated to equal the simultaneous rate of energy utilization.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed1984

Purified diets: some cautions about casein.

Growth and intake of weanling rats on five casein-based purified diets and matched cereal-based diets were compared. The results support Lát's conjecture that the failure of animals to exhibit normal growth on some purified diets may be attributed to their failure to consume sufficient casein. Given a choice, the rats consumed both types of food, composing a diet in which the ratio of purified to cereal-based diet was 2:1, and they grew normally. Although the growth-promoting characteristics of caseins from different sources varied, the preference ratio between casein- and cereal-based diets was the same with one exception: a reduced preference for purified diet was shown by animals who had previously experienced subnormal growth for an extended period of time on a purified diet. These results show that all caseins are not equivalent in their growth-promoting properties. Further, they show that rats are exquisitely sensitive to the nutritional properties of their diets and, given the opportunity, can compose a diet which yields normal growth.

Animal Feed↗
PubMed1975

Murine mammary gland RNA directed synthesis of casein in a heterologous cell-free protein synthesis system.

A cell-free protein synthesis system derived from Ehrlich ascites tumor cell ribosomes (S30) plus rabbit reticulocyte tRNA was developed and the activity of the system was dependent on rabbit reticulocyte ribosomal salt (0.5 M KC1) wash factors, The exogenous mRNAs from BALB/c mouse liver and the mammary gland were translated with a high efficiency in this heterologous cell-free system. Furthermore, the RNA from the lactating mammary gland faithfully directed the synthesis of casein. The presence of mouse casein in the reaction product was identified by radioimmunoprecipitation with mouse casein antiserum, co-electrophoresis of the reaction product and mouse casein the urea-polyacrylamide gel and by electrophoresis in sodium dodecyl sulfate (SDS) polyacrylamide gel. The major portion of the lactating mammary gland RNA directed synthesis of the milk protein in the cell-free system appeared to be analogous to alphas casein,

Animals↗
PubMed1983

NMR studies of the phosphoserine regions of bovine alpha s1- and beta-casein. Assignment of 31P resonances to specific phosphoserines and cation binding studied by measurement of enhancement of 1H relaxation rate.

(1) High-resolution 31P-NMR was used to study the environment of the phosphoserine residues of the phosphoproteins, alpha s1-casein B, beta-casein A2 and beta-casein C. For reference purposes 31P-NMR spectra of phosvitin and ovalbumin were also collected. (2) 31P resonances were assigned to specific phosphoserine residues as a result of comparisons of the high-resolution 31P-NMR spectra for alpha s1- and beta-caseins and for peptide fragments of these proteins obtained by cyanogen bromide and trypsin cleavage. (3) Measurements of the enhancement of the relaxation rate for water protons (1H) on addition of Mn2+ to alpha s1-casein B and to a fragment alpha s1-CN3, obtained by cyanogen bromide cleavage, gave approximate pK values for the binding groups and suggest the possibility of a conformational change induced by varying the concentration of divalent cation.

Animals↗
PubMed1985

The rennet-induced clotting of para-kappa-casein revisited: inhibition experiments with pepstatin A.

The proteolysis of micellar kappa-casein by rennet was followed by SDS-polyacrylamide gel-electrophoresis and the clotting of the para-kappa-casein formed by absorbance measurements. Up to a degree of proteolysis of about 0.4 the enzyme-inhibitor pepstatin A proved able to instantaneously stop the clotting. This effect is explained by the rapid condensation of monofunctional, monomeric and polymeric particles of para-kappa-casein. At higher degrees of proteolysis pepstatin was no longer able to completely block the polymerization. This is explained by the retardation of the condensation of the monofunctionals as their size grows larger. A kinetic analysis of the enzyme-controlled stage of the clotting process predicts that the system should gel at an early degree of proteolysis of about 0.07. The actual gel points occur at considerably higher degrees of proteolysis. This suggests that the enzymic attack of the polymeric inert kappa-casein particles is not completely at random. Primary micelles of kappa-casein, however, are degraded by random attack rather than by a 'catch-and-razor' mechanism.

Caseins↗
PubMed1996

Action on bovine alpha s1-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L.

The cleavage of purified bovine alpha s1-casein separately by cardosin A and cardosin B, two distinct milk-clotting aspartic proteinases (APs) present in the stigmas of the plant Cynara cardunculus L., was studied. Casein digestion peptides were separated either by SDS-PAGE or by reverse-phase HPLC, and their N-terminal amino acid sequences were subsequently determined by automated Edman degradation, thus identifying the cleavage sites. Results showed that both enzymes exert a similar but distinct action on bovine alpha s1-casein. In common they have the preference for the bond Phe23-Phe24, and the cleavage of Trp164-Tyr165 and Phe153-Tyr154. Cardosin A also cleaves the bond Tyr165-Tyr166, whereas Cardosin B cleaves an extra type of bond, Phe150-Arg151, revealing a slightly broader specificity. A model for the action of both enzymes on bovine alpha s1-casein is proposed and discussed. In comparison with the reported action of chymosin on bovine alpha s1-casein, both cardosins proved to have a broader specificity towards this particular substrate due to a higher ability to cleave bonds between residues with large hydrophobic side-chains.

Animals↗
PubMed1988

Phosphorylation of phosvitin by casein kinase-2 provides the evidence that phosphoserines can replace carboxylic amino acids as specificity determinants.

The consensus sequence of casein kinase-2 consists of a serine (threonine) followed by a cluster of glutamic and/or aspartic acids, the one at position +3 playing an especially crucial role (Marin et al., (1986) Eur. J. Biochem. 160, 239-244 and Kuenzel et al. (1987) J. Biol. Chem. 262, 9136-9140). None of the 123 serines of the main phosvitin component (34 kDa) fulfils such a requirement (Byrne et al. (1984) Biochemistry 23, 4275-4279), rather, most of them are clustered into stretches of up to 14 entirely phosphorylated residues. Three out of the four threonines lie close to the N-terminal side of such phosphoseryl blocks. Here we show that native 34 kDa phosvitin is a poor substrate of casein kinase-2, its radiolabeling occurring mostly at threonine residue(s); a very slight (1%) previous dephosphorylation with acid phosphatase converts phosvitin into an excellent substrate for casein kinase-2, its phosphorylation occurring almost exclusively at serine residues. Extensive dephosphorylation however (greater than 40%) reduces the phosphorylation efficiency of casein kinase-2. These results show that phosphoserine residues can replace carboxylic residues as specificity determinants for casein kinase-2.

Amino Acids↗
PubMed1992

Substrate-specific modulation of Src-mediated phosphorylation of Ras and caseins by sphingosines and other substrate modulators.

It is important for the understanding of protein kinase action to differentiate between regulation at the enzyme and at the substrate levels. For example, the inhibitors dinitrophenol-tyrosine and tyrphostins act at the enzyme level to inhibit phosphorylation of all substrates by c-Src and v-Src kinases. In contrast, polylysine acts at the substrate level to stimulate Src-mediated phosphorylation of beta-casein but to inhibit phosphorylation of alpha-casein. Here we demonstrate novel enzyme-specific and substrate-specific modulations of Src kinase activity of potential physiological significance. At the enzyme level, we observed that c-Src kinase preferentially phosphorylates alpha-casein, while the v-Src kinase prefers beta-casein. At the substrate level we observed substrate-specific modulation by physiological factors including sphingosine, sphingosine derivatives and the ganglioside GM3. Galactosyl-sphingosine (psychosine) was more effective in stimulating phosphorylation of beta-casein and poly(E1A1Y1) than sphingosine. Glucosyl- and lactosyl-sphingosine were ineffective. Rat was extensively phosphorylated by c-Src in the presence of polylysine, and to a lesser extent in the sphingosine and galactosyl-sphingosine. These unexpected differences point out another potential mechanism for regulation of c-Src and v-Src kinase activities and may help to explain some of the pleotyptic manifestations of protein tyrosine kinase actions.

Animals↗
PubMed1996

Continuous production of high degree casein hydrolysates by immobilized proteases in column reactor.

The enzymatic complete hydrolysis of casein was investigated by using immobilized endopeptidase and exopeptidase packed in the jacketed column reactors. The mass transfer efficiency of proteins was improved by using sliced shrimp chitin hull as enzyme support, which formed a network structure inside the column reactor that prevented the formation of protein precipitate and increased the line flow rate of protein solution. The specificity of the protease was of crucial importance for both the hydrolysis degree and the free amino acid content of the hydrolysates. Of the enzymes, tested, the immobilized A. oryzae protease was the most effective enzyme in breaking down the casein molecules and releasing the free amino acid from casein hydrolysates. The immobilized pancreatic and kidney exopeptidase could lead to a 20% increase of free amino acids. The free amino acid content of casein hydrolysates was 34.81% after processing and could reach to 64% if the column length was doubled, but 100% hydrolysis was impossible as the reverse reaction was also taking place. The casein hydrolysates was characterized by its high degree of hydrolysis and high content of free amino acids. It can be applied in infant formula, element diet, and as a protein ingredient for food industry.

Amino Acids↗